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2016 ; 116
(11
): 6503-15
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Protein Allostery and Conformational Dynamics
#MMPMID26876046
Guo J
; Zhou HX
Chem Rev
2016[Jun]; 116
(11
): 6503-15
PMID26876046
show ga
The functions of many proteins are regulated through allostery, whereby effector
binding at a distal site changes the functional activity (e.g., substrate binding
affinity or catalytic efficiency) at the active site. Most allosteric studies
have focused on thermodynamic properties, in particular, substrate binding
affinity. Changes in substrate binding affinity by allosteric effectors have
generally been thought to be mediated by conformational transitions of the
proteins or, alternatively, by changes in the broadness of the free energy basin
of the protein conformational state without shifting the basin minimum position.
When effector binding changes the free energy landscape of a protein in
conformational space, the change affects not only thermodynamic properties but
also dynamic properties, including the amplitudes of motions on different time
scales and rates of conformational transitions. Here we assess the roles of
conformational dynamics in allosteric regulation. Two cases are highlighted where
NMR spectroscopy and molecular dynamics simulation have been used as
complementary approaches to identify residues possibly involved in allosteric
communication. Perspectives on contentious issues, for example, the relationship
between picosecond-nanosecond local and microsecond-millisecond conformational
exchange dynamics, are presented.
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